ID   SYGA_YERPG              Reviewed;         304 AA.
AC   A9R4G0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN   OrderedLocusNames=YpAngola_A3783;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR   EMBL; CP000901; ABX87301.1; -; Genomic_DNA.
DR   RefSeq; WP_002209624.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R4G0; -.
DR   SMR; A9R4G0; -.
DR   GeneID; 66843666; -.
DR   KEGG; ypg:YpAngola_A3783; -.
DR   PATRIC; fig|349746.12.peg.496; -.
DR   OMA; SYYQFQV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..304
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000101250"
SQ   SEQUENCE   304 AA;  34758 MW;  544CCA56FD1DE47D CRC64;
     MQKFDTKTFQ GLILTLQDYW ARQGCTIVQP LDMEVGAGTS HPMTCLRAIG PEPIAAAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVIIKPS PDNIQELYLG SLKELGLDPT IHDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGLERL AMYIQGVDSV
     YDLIWCDGPL GTTTYGDIYH QNEVEQSTYN FEYADVDFLF SCFEQYEKEA QSLLALETPL
     PLPAYERILK AGHTFNLLDA RKAISVTERQ RYILRIRTLT KAVAEAYYAS REALGFPMCK
     KNQN